Follistatin and Noggin Are Excluded from the Zebrafish Organizer
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Spemann Organizer Transcriptome Induction by Early Beta-Catenin, Wnt
Spemann organizer transcriptome induction by early PNAS PLUS beta-catenin, Wnt, Nodal, and Siamois signals in Xenopus laevis Yi Dinga,b,1, Diego Plopera,b,1, Eric A. Sosaa,b, Gabriele Colozzaa,b, Yuki Moriyamaa,b, Maria D. J. Beniteza,b, Kelvin Zhanga,b, Daria Merkurjevc,d,e, and Edward M. De Robertisa,b,2 aHoward Hughes Medical Institute, University of California, Los Angeles, CA 90095-1662; bDepartment of Biological Chemistry, University of California, Los Angeles, CA 90095-1662; cDepartment of Medicine, University of California, Los Angeles, CA 90095-1662; dDepartment of Microbiology, University of California, Los Angeles, CA 90095-1662; and eDepartment of Human Genetics, University of California, Los Angeles, CA 90095-1662 Contributed by Edward M. De Robertis, February 24, 2017 (sent for review January 17, 2017; reviewed by Juan Larraín and Stefano Piccolo) The earliest event in Xenopus development is the dorsal accumu- Wnt8 mRNA leads to a dorsalized phenotype consisting entirely of lation of nuclear β-catenin under the influence of cytoplasmic de- head structures without trunks and a radial Spemann organizer terminants displaced by fertilization. In this study, a genome-wide (9–11). Similar dorsalizing effects are obtained by incubating approach was used to examine transcription of the 43,673 genes embryos in lithium chloride (LiCl) solution at the 32-cell stage annotated in the Xenopus laevis genome under a variety of con- (12). LiCl mimics the early Wnt signal by inhibiting the enzymatic ditions that inhibit or promote formation of the Spemann orga- activity of glycogen synthase kinase 3 (GSK3) (13), an enzyme nizer signaling center. -
Bmpr Encodes a Type I Bone Morphogenetic Protein Receptor That Is Essential for Gastrulation During Mouse Embryogenesis
Downloaded from genesdev.cshlp.org on October 8, 2021 - Published by Cold Spring Harbor Laboratory Press Bmpr encodes a type I bone morphogenetic protein receptor that is essential for gastrulation during mouse embryogenesis Yuji Mishina, ~ Atsushi Suzuki, 2 Naoto Ueno, 2 and Richard R. Behringer ~'3 1Department of Molecular Genetics, The University of Texas, M.D. Anderson Cancer Center, Houston, Texas 77030 USA; ~Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060, Japan Bone morphogenetic proteins (BMPs) are secreted proteins that interact with cell-surface receptors and are believed to play a variety of important roles during vertebrate embryogenesis. Bmpr, also known as ALK-3 and Brk-1, encodes a type I transforming growth factor-~ (TGF-[3) family receptor for BMP-2 and BMP-4. Bmpr is expressed ubiquitously during early mouse embryogenesis and in most adult mouse tissues. To study the function of Bmpr during mammalian development, we generated Bmpr-mutant mice. After embryonic day 9.5 (E9.5), no homozygous mutants were recovered from heterozygote matings. Homozygous mutants with morphological defects were first detected at E7.0 and were smaller than normal. Morphological and molecular examination demonstrated that no mesoderm had formed in the mutant embryos. The growth characteristics of homozygous mutant blastocysts cultured in vitro were indistinguishable from those of controls; however, embryonic ectoderm (epiblast) cell proliferation was reduced in all homozygous mutants at E6.5 before morphological abnormalities had become prominent. Teratomas arising from E7.0 mutant embryos contained derivatives from all three germ layers but were smaller and gave rise to fewer mesodermal cell types, such as muscle and cartilage, than controls. -
Access AMH Instructions for Use Anti-Müllerian Hormone (AMH) © 2017 Beckman Coulter, Inc
ACCESS Immunoassay Systems Access AMH Instructions For Use Anti-Müllerian hormone (AMH) © 2017 Beckman Coulter, Inc. All rights reserved. B13127 FOR PROFESSIONAL USE ONLY Rx Only ANNUAL REVIEW Reviewed by Date Reviewed by Date PRINCIPLE INTENDED USE The Access AMH assay is a paramagnetic particle chemiluminescent immunoassay for the quantitative determination of anti-Müllerian hormone (AMH) levels in human serum and lithium heparin plasma using the Access Immunoassay Systems as an aid in the assessment of ovarian reserve in women presenting to fertility clinics. This system is intended to distinguish between women presenting with AFC (antral follicle count) values > 15 (high ovarian reserve) and women with AFC values ≤ 15 (normal or diminished ovarian reserve). The Access AMH is intended to be used in conjunction with other clinical and laboratory findings such as antral follicle count, before starting fertility therapy. The Access AMH is not intended to be used for monitoring of women undergoing controlled ovarian stimulation in an Assisted Reproduction Technology program. SUMMARY AND EXPLANATION Anti-Müllerian hormone (AMH) is a glycoprotein, which circulates as a dimer composed of two identical 72 kDa monomers that are linked by disulfide bridges. AMH belongs to the transforming growth factor-β family.1,2 AMH is named for its first described function in fetal sexual differentiation: a regression of the Müllerian ducts in males during early fetal life. In males, AMH is secreted by Sertoli cells of the testes. AMH concentrations are high -
Nodal Signaling Is Required for Mesodermal and Ventral but Not For
© 2015. Published by The Company of Biologists Ltd | Biology Open (2015) 4, 830-842 doi:10.1242/bio.011809 RESEARCH ARTICLE Nodal signaling is required for mesodermal and ventral but not for dorsal fates in the indirect developing hemichordate, Ptychodera flava Eric Röttinger1,2,3,*, Timothy Q. DuBuc4, Aldine R. Amiel1,2,3 and Mark Q. Martindale4 ABSTRACT early fate maps of direct and indirect developing hemichordates, are Nodal signaling plays crucial roles in vertebrate developmental similar to those of indirect-developing echinoids (Colwin and processes such as endoderm and mesoderm formation, and axial Colwin, 1951; Cameron et al., 1987; Cameron et al., 1989; Cameron patterning events along the anteroposterior, dorsoventral and left- and Davidson, 1991; Henry et al., 2001). While the bilaterally right axes. In echinoderms, Nodal plays an essential role in the symmetric echinoderm larvae exhibit strong similarities to establishment of the dorsoventral axis and left-right asymmetry, but chordates in axial patterning and germ layer specification events, not in endoderm or mesoderm induction. In protostomes, Nodal adult body plan comparisons in echinoderms have been difficult due signaling appears to be involved only in establishing left-right to their unique adult pentaradial symmetry. However, both the larval asymmetry. Hence, it is hypothesized that Nodal signaling has and adult body plans of enteropneust hemichordates are bilaterally been co-opted to pattern the dorsoventral axis of deuterostomes and symmetric, and larvae from indirect developing hemichordates for endoderm, mesoderm formation as well as anteroposterior such as Ptychodera flava (P. flava) share similarities in patterning in chordates. Hemichordata, together with echinoderms, morphology, axial organization, and developmental fate map with represent the sister taxon to chordates. -
Differential Compartmentalization of BMP4/NOGGIN Requires NOGGIN Trans-Epithelial Transport
bioRxiv preprint doi: https://doi.org/10.1101/2020.12.18.423440; this version posted December 19, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-ND 4.0 International license. Differential compartmentalization of BMP4/NOGGIN requires NOGGIN trans-epithelial transport Tien Phan-Everson1-2 +, Fred Etoc1 +, Ali H. Brivanlou1 *, Eric D. Siggia2 * 1 Laboratory of Stem Cell Biology and Molecular Embryology, The Rockefeller University, New York, New York 10065, USA. 2 Laboratory of Physical, Mathematical, and Computational Biology, The Rockefeller University, New York, New York 10065, USA. + Co-first Authors * Joint Corresponding Authors Correspondence: [email protected]; [email protected] Summary Using self-organizing human models of gastrulation, we previously showed that (i) BMP4 initiates the cascade of events leading to gastrulation; (ii) BMP4 signal-reception is restricted to the basolateral domain; and (iii) in a human-specific manner, BMP4 directly induces the expression of NOGGIN. Here, we report the surprising discovery that in human epiblasts, NOGGIN and BMP4 were secreted into opposite extracellular spaces. Interestingly, apically-presented NOGGIN could inhibit basally-delivered BMP4. Apically-imposed microfluidic flow demonstrated that NOGGIN traveled in the apical extracellular space. Our co-localization analysis detailed the endocytotic route that trafficked NOGGIN from the apical space to the basolateral intercellular space where BMP4 receptors were located. This apical-to-basal transcytosis was indispensable for NOGGIN inhibition. Taken together, the segregation of activator/inhibitor into distinct extracellular spaces challenges classical views of morphogen movement. -
Downloaded from Bioscientifica.Com at 10/03/2021 07:38:50PM Via Free Access
229 3 <V>:<Iss> X ZHOU and others Gonadotrope-specific Bmpr1a 229229:3:3 331–341 Research knockout mice Normal gonadotropin production and fertility in gonadotrope- specific Bmpr1a knockout mice Xiang Zhou1,2, Ying Wang1,2, Luisina Ongaro1,2, Ulrich Boehm3, Vesa Kaartinen4, Yuji Mishina4 and Daniel J Bernard1,2 1Department of Pharmacology and Therapeutics, McGill University, Montreal, Québec, Canada 2Centre for Research in Reproduction and Development, McGill University, Montreal, Québec, Canada Correspondence 3Department of Pharmacology and Toxicology, University of Saarland School of Medicine, Homburg, Germany should be addressed 4Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, to D J Bernard Michigan, USA Email [email protected] Abstract Pituitary follicle-stimulating hormone (FSH) synthesis is regulated by transforming Key Words growth factor β superfamily ligands, most notably the activins and inhibins. Bone f pituitary morphogenetic proteins (BMPs) also regulate FSHβ subunit (Fshb) expression in f FSH immortalized murine gonadotrope-like LβT2 cells and in primary murine or ovine f bone morphogenetic Endocrinology primary pituitary cultures. BMP2 signals preferentially via the BMP type I receptor, protein of BMPR1A, to stimulate murine Fshb transcription in vitro. Here, we used a Cre–lox f activin receptor-like kinase approach to assess BMPR1A’s role in FSH synthesis in mice in vivo. Gonadotrope- Journal f Cre-lox specific Bmpr1a knockout animals developed normally and had reproductive organ weights comparable with those of controls. Knockouts were fertile, with normal serum gonadotropins and pituitary gonadotropin subunit mRNA expression. Cre-mediated recombination of the floxed Bmpr1a allele was efficient and specific, as indicated by PCR analysis of diverse tissues and isolated gonadotrope cells. -
Inhibitory Effects of Activin on the Growth and Morphogenesis of Primary and Transformed Mammary Epithelial Cells'
ICANCERRESEARCH56. I 155-I 163. March I. 19961 Inhibitory Effects of Activin on the Growth and Morphogenesis of Primary and Transformed Mammary Epithelial Cells' Qiu Yan Liu, Birunthi Niranjan, Peter Gomes, Jennifer J. Gomm, Derek Davies, R. Charles Coombes, and Lakjaya Buluwela2 Departments of Medical Oncology (Q. Y. L, P. G.. J. J. G., R. C. C., L B.J and Biochemistry (Q. Y. L. L B.J. Charing Cross and Westminster Medical School, Fuiham Palace Road. London W6 8RF; Division of Cell Biology and Experimental Pathology. Institute of Cancer Research, 15 Cotswald Rood, Sutton. Surrey SM2 SNG (B. NJ; and FACS Analysis Laboratory. imperial Cancer Research Fund, Lincoln ‘sInnFields. London WC2A 3PX (D. DI, United Kingdom ABSTRACT logical activities of activin. Indeed, two types of activin receptors have aLready been identified in the mouse (28) and several forms in Activin Is a member of the transforming growth factor fi superfamily, Xenopus (29, 30). The sequences of the Act-RI! (3 1), the TGF-@ type which is known to have activities Involved In regulating differentiation II receptor (32), the TGF-f3 type I receptor (33), and various activin and development. By using reverse transcrlption.PCR analysis on immu noafflnity.purlfied human breast cells, we have found that activin IJa and receptor-like genes (34) have been described. The comparison of these activin type II receptor are expressed by myoepithelial cells, whereas no sequences shows that they belong to a newly defined family of expression was detected In other breast cell types. In examining 15 breast membrane-bound, ligand-activated serine-threonine kinases (35). -
Inhibition of Activin/Nodal and Wnt Signaling Andrey V
RESEARCH ARTICLE 5345 Development 138, 5345-5356 (2011) doi:10.1242/dev.068908 © 2011. Published by The Company of Biologists Ltd Novel functions of Noggin proteins: inhibition of Activin/Nodal and Wnt signaling Andrey V. Bayramov*, Fedor M. Eroshkin*, Natalia Y. Martynova, Galina V. Ermakova, Elena A. Solovieva and Andrey G. Zaraisky‡ SUMMARY The secreted protein Noggin1 is an embryonic inducer that can sequester TGF cytokines of the BMP family with extremely high affinity. Owing to this function, ectopic Noggin1 can induce formation of the headless secondary body axis in Xenopus embryos. Here, we show that Noggin1 and its homolog Noggin2 can also bind, albeit less effectively, to ActivinB, Nodal/Xnrs and XWnt8, inactivation of which, together with BMP, is essential for the head induction. In support of this, we show that both Noggin proteins, if ectopically produced in sufficient concentrations in Xenopus embryo, can induce a secondary head, including the forebrain. During normal development, however, Noggin1 mRNA is translated in the presumptive forebrain with low efficiency, which provides the sufficient protein concentration for only its BMP-antagonizing function. By contrast, Noggin2, which is produced in cells of the anterior margin of the neural plate at a higher concentration, also protects the developing forebrain from inhibition by ActivinB and XWnt8 signaling. Thus, besides revealing of novel functions of Noggin proteins, our findings demonstrate that specification of the forebrain requires isolation of its cells from BMP, Activin/Nodal and Wnt signaling not only during gastrulation but also at post-gastrulation stages. KEY WORDS: Noggin, Activin, Nodal, Wnt, Forebrain, Xenopus INTRODUCTION laevis embryos, to bind to and antagonize several secreted proteins The secreted protein Noggin (Noggin1) was first discovered in known to be involved in regulation of TGF and Wnt signaling. -
Signal Transduction Pathway Through Activin Receptors As a Therapeutic Target of Musculoskeletal Diseases and Cancer
Endocr. J./ K. TSUCHIDA et al.: SIGNALING THROUGH ACTIVIN RECEPTORS doi: 10.1507/endocrj.KR-110 REVIEW Signal Transduction Pathway through Activin Receptors as a Therapeutic Target of Musculoskeletal Diseases and Cancer KUNIHIRO TSUCHIDA, MASASHI NAKATANI, AKIYOSHI UEZUMI, TATSUYA MURAKAMI AND XUELING CUI Division for Therapies against Intractable Diseases, Institute for Comprehensive Medical Science (ICMS), Fujita Health University, Toyoake, Aichi 470-1192, Japan Received July 6, 2007; Accepted July 12, 2007; Released online September 14, 2007 Correspondence to: Kunihiro TSUCHIDA, Institute for Comprehensive Medical Science (ICMS), Fujita Health University, Toyoake, Aichi 470-1192, Japan Abstract. Activin, myostatin and other members of the TGF-β superfamily signal through a combination of type II and type I receptors, both of which are transmembrane serine/threonine kinases. Activin type II receptors, ActRIIA and ActRIIB, are primary ligand binding receptors for activins, nodal, myostatin and GDF11. ActRIIs also bind a subset of bone morphogenetic proteins (BMPs). Type I receptors that form complexes with ActRIIs are dependent on ligands. In the case of activins and nodal, activin receptor-like kinases 4 and 7 (ALK4 and ALK7) are the authentic type I receptors. Myostatin and GDF11 utilize ALK5, although ALK4 could also be activated by these growth factors. ALK4, 5 and 7 are structurally and functionally similar and activate receptor-regulated Smads for TGF-β, Smad2 and 3. BMPs signal through a combination of three type II receptors, BMPRII, ActRIIA, and ActRIIB and three type I receptors, ALK2, 3, and 6. BMPs activate BMP-specific Smads, Smad1, 5 and 8. Smad proteins undergo multimerization with co-mediator Smad, Smad4, and translocated into the nucleus to regulate the transcription of target genes in cooperation with nuclear cofactors. -
Supplementary Materials
Supplementary Materials + - NUMB E2F2 PCBP2 CDKN1B MTOR AKT3 HOXA9 HNRNPA1 HNRNPA2B1 HNRNPA2B1 HNRNPK HNRNPA3 PCBP2 AICDA FLT3 SLAMF1 BIC CD34 TAL1 SPI1 GATA1 CD48 PIK3CG RUNX1 PIK3CD SLAMF1 CDKN2B CDKN2A CD34 RUNX1 E2F3 KMT2A RUNX1 T MIXL1 +++ +++ ++++ ++++ +++ 0 0 0 0 hematopoietic potential H1 H1 PB7 PB6 PB6 PB6.1 PB6.1 PB12.1 PB12.1 Figure S1. Unsupervised hierarchical clustering of hPSC-derived EBs according to the mRNA expression of hematopoietic lineage genes (microarray analysis). Hematopoietic-competent cells (H1, PB6.1, PB7) were separated from hematopoietic-deficient ones (PB6, PB12.1). In this experiment, all hPSCs were tested in duplicate, except PB7. Genes under-expressed or over-expressed in blood-deficient hPSCs are indicated in blue and red respectively (related to Table S1). 1 C) Mesoderm B) Endoderm + - KDR HAND1 GATA6 MEF2C DKK1 MSX1 GATA4 WNT3A GATA4 COL2A1 HNF1B ZFPM2 A) Ectoderm GATA4 GATA4 GSC GATA4 T ISL1 NCAM1 FOXH1 NCAM1 MESP1 CER1 WNT3A MIXL1 GATA4 PAX6 CDX2 T PAX6 SOX17 HBB NES GATA6 WT1 SOX1 FN1 ACTC1 ZIC1 FOXA2 MYF5 ZIC1 CXCR4 TBX5 PAX6 NCAM1 TBX20 PAX6 KRT18 DDX4 TUBB3 EPCAM TBX5 SOX2 KRT18 NKX2-5 NES AFP COL1A1 +++ +++ 0 0 0 0 ++++ +++ ++++ +++ +++ ++++ +++ ++++ 0 0 0 0 +++ +++ ++++ +++ ++++ 0 0 0 0 hematopoietic potential H1 H1 H1 H1 H1 H1 PB6 PB6 PB7 PB7 PB6 PB6 PB7 PB6 PB6 PB6.1 PB6.1 PB6.1 PB6.1 PB6.1 PB6.1 PB12.1 PB12.1 PB12.1 PB12.1 PB12.1 PB12.1 Figure S2. Unsupervised hierarchical clustering of hPSC-derived EBs according to the mRNA expression of germ layer differentiation genes (microarray analysis) Selected ectoderm (A), endoderm (B) and mesoderm (C) related genes differentially expressed between hematopoietic-competent (H1, PB6.1, PB7) and -deficient cells (PB6, PB12.1) are shown (related to Table S1). -
Novel Roles of Follistatin/Myostatin in Transforming Growth Factor-Β
UCLA UCLA Previously Published Works Title Novel Roles of Follistatin/Myostatin in Transforming Growth Factor-β Signaling and Adipose Browning: Potential for Therapeutic Intervention in Obesity Related Metabolic Disorders. Permalink https://escholarship.org/uc/item/2sv437dw Authors Pervin, Shehla Reddy, Srinivasa T Singh, Rajan Publication Date 2021 DOI 10.3389/fendo.2021.653179 Peer reviewed eScholarship.org Powered by the California Digital Library University of California REVIEW published: 09 April 2021 doi: 10.3389/fendo.2021.653179 Novel Roles of Follistatin/Myostatin in Transforming Growth Factor-b Signaling and Adipose Browning: Potential for Therapeutic Intervention in Obesity Related Metabolic Disorders Shehla Pervin 1,2, Srinivasa T. Reddy 3,4 and Rajan Singh 1,2,5* 1 Department of Obstetrics and Gynecology, David Geffen School of Medicine at University of California Los Angeles (UCLA), Los Angeles, CA, United States, 2 Division of Endocrinology and Metabolism, Charles R. Drew University of Medicine and Edited by: Science, Los Angeles, CA, United States, 3 Department of Molecular and Medical Pharmacology, David Geffen School of Xinran Ma, Medicine at UCLA, Los Angeles, CA, United States, 4 Department of Medicine, Division of Cardiology, David Geffen School of East China Normal University, China Medicine, University of California Los Angeles, Los Angeles, CA, United States, 5 Department of Endocrinology, Men’s ’ Reviewed by: Health: Aging and Metabolism, Brigham and Women s Hospital, Boston, MA, United States Meng Dong, Institute of Zoology, Chinese Obesity is a global health problem and a major risk factor for several metabolic conditions Academy of Sciences (CAS), China Abir Mukherjee, including dyslipidemia, diabetes, insulin resistance and cardiovascular diseases. -
Lack of Tgfbr1 and Acvr1b Synergistically Stimulates Myofibre Hypertrophy And
bioRxiv preprint doi: https://doi.org/10.1101/2021.03.03.433740; this version posted March 6, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Lack of Tgfbr1 and Acvr1b synergistically stimulates myofibre hypertrophy and accelerates muscle regeneration *M.M.G. Hillege1, *A. Shi1,2 ,3, R.C. Galli Caro1, G. Wu4, P. Bertolino5, W.M.H. Hoogaars1,6, R.T. Jaspers1 1. Laboratory for Myology, Department of Human Movement Sciences, Faculty of Behavioural and Movement Sciences, Vrije Universiteit Amsterdam, Amsterdam Movement Sciences, Amsterdam, The Netherlands 2. Department of Oral and Maxillofacial Surgery/Pathology, Amsterdam UMC and Academic Center for Dentistry Amsterdam (ACTA), Vrije Universiteit Amsterdam (VU), Amsterdam Movement Sciences (AMS), Amsterdam, the Netherlands 3. Key Laboratory of Oral Medicine, Guangzhou Institute of Oral Disease, Affiliated Stomatology Hospital of Guangzhou Medical University, Guangzhou Medical University, Guangzhou, China 4. Department of Oral Implantology and Prosthetic Dentistry, Academic Centre for Dentistry Amsterdam (ACTA), University of Amsterdam (UvA) and Vrije Universiteit Amsterdam (VU), The Netherlands 5. Centre de Recherche en Cancérologie de Lyon, UMR INSERM U1052/CNRS 5286, Université de Lyon, Centre Léon Bérard, Lyon, France 6. European Research Institute for the Biology of Ageing (ERIBA), University Medical Center Groningen (UMCG), University of Groningen, Groningen, The Netherlands *Contributed equally to this manuscript **Correspondence: [email protected]; Tel.: +31 (0) 205988463 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.03.03.433740; this version posted March 6, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder.